BRENDA - Enzyme Database show
show all sequences of 4.1.3.3

Structural insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with gamma-thialysine by using a chemical mutagenesis strategy

Timms, N.; Windle, C.L.; Polyakova, A.; Ault, J.R.; Trinh, C.H.; Pearson, A.R.; Nelson, A.; Berry, A.; ChemBioChem 14, 474-481 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene nanA, recombinant expression of His6-tagged wild-type and mutant enzymes from plasmid pKK223-3 in Escherichia coli strain BL21(DE3)
Staphylococcus aureus
Crystallization (Commentary)
Crystallization
Organism
purified recombinant wild-type enzyme and mutants K165C variant and K165-gamma-thialysine, alone or in complex with pyruvate, hanging drop vapour diffusion method, mixing of 0.002 ml of protein solution containing 8 mg/ml protein in 50 mM, pH 7.4, with 0.002 ml of reservoir solution containing 100 mM Tris-HCl, pH 7.0-8.5, 200 mM NaCl, and 18-28% w/v PEG 3350, pyruvate complexes of the wild-type and K165-gamma-thialysine mutant enzymes crystals are soaked in the mother liquor containing 100 mM sodium pyruvate and 15% v/v PEG 400 for 1 min before being sequentially transferred to mother liquor with 5% increments in PEG 400 concentration. The final soak contains the mother liquor containing 100 mM sodium pyruvate and 25% v/v PEG 400, 18°C, X-ray diffraction structure determination and analysis at about 2.0 A resolution, molecular replacement
Staphylococcus aureus
Engineering
Amino acid exchange
Commentary
Organism
C118A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C118S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C238A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C238S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C270A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C270S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C82A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C82S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
K165C
site-directed mutagenesis to introduce a cysteine in place of Lys165 in the enzyme active site and complete conversion of the cysteine into gamma-thialysine through dehydroalanine as by chemical mutagenesis, ESI-mass spectrometry and kinetic characterisation, the K165C variant is severely impaired in catalysis, kcat/Km is reduced 720fold compared with wild-type
Staphylococcus aureus
K165Dha
site-directed mutagenesis to introduce a cysteine in place of Lys165 in the enzyme active site and complete conversion of the cysteine into gamma-thialysine, Dha, through dehydroalanine as by chemical mutagenesis, ESI-mass spectrometry and kinetic characterisation, the enzyme containing gamma-thialysine regains 17-30% of the wild-type activity
Staphylococcus aureus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.013
-
N-acetylneuraminate
purified recombinant mutant K165C, pH 7.4, 30°C
Staphylococcus aureus
0.015
-
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 6.8, 30°C
Staphylococcus aureus
0.023
-
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 7.4, 30°C
Staphylococcus aureus
0.036
-
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 7.4, 30°C
Staphylococcus aureus
0.04
-
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 6.8, 30°C
Staphylococcus aureus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33992
-
x * 33992, recombinant His6-tagged wild-type enzyme, mass spectrometry
Staphylococcus aureus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N-acetylneuraminate
Staphylococcus aureus
-
N-acetyl-D-mannosamine + pyruvate
-
-
r
N-acetylneuraminate
Staphylococcus aureus NCTC 8325
-
N-acetyl-D-mannosamine + pyruvate
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Staphylococcus aureus
Q2G160
gene nanA
-
Staphylococcus aureus NCTC 8325
Q2G160
gene nanA
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Staphylococcus aureus
Renatured (Commentary)
Commentary
Organism
recombinant wild-type enzyme with various concentrations of urea in Tris·HCl buffer, 50 mM, pH 7.4, the refolded enzyme shows higher activity than the native wild-type enzyme
Staphylococcus aureus
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.33
-
purified recombinant wild-type enzyme, pH 7.4, 30°C
Staphylococcus aureus
6
-
purified recombinant refolded wild-type enzyme, pH 7.4, 30°C
Staphylococcus aureus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N-acetylneuraminate
-
727317
Staphylococcus aureus
N-acetyl-D-mannosamine + pyruvate
-
-
-
r
N-acetylneuraminate
-
727317
Staphylococcus aureus NCTC 8325
N-acetyl-D-mannosamine + pyruvate
-
-
-
r
Subunits
Subunits
Commentary
Organism
?
x * 33992, recombinant His6-tagged wild-type enzyme, mass spectrometry
Staphylococcus aureus
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Staphylococcus aureus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.013
-
N-acetylneuraminate
purified recombinant mutant K165C, pH 7.4, 30°C
Staphylococcus aureus
0.015
-
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 6.8, 30°C
Staphylococcus aureus
0.023
-
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 7.4, 30°C
Staphylococcus aureus
0.036
-
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 7.4, 30°C
Staphylococcus aureus
0.04
-
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 6.8, 30°C
Staphylococcus aureus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.8
-
mutant K165-gamma-thialysine
Staphylococcus aureus
7.4
-
wild-type enzyme
Staphylococcus aureus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
5
10
pH-activity profiles of the wild-type enzyme, overview
Staphylococcus aureus
6
9
pH-activity profiles of the K165-gamma-thialysine mutant enzyme, overview
Staphylococcus aureus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene nanA, recombinant expression of His6-tagged wild-type and mutant enzymes from plasmid pKK223-3 in Escherichia coli strain BL21(DE3)
Staphylococcus aureus
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified recombinant wild-type enzyme and mutants K165C variant and K165-gamma-thialysine, alone or in complex with pyruvate, hanging drop vapour diffusion method, mixing of 0.002 ml of protein solution containing 8 mg/ml protein in 50 mM, pH 7.4, with 0.002 ml of reservoir solution containing 100 mM Tris-HCl, pH 7.0-8.5, 200 mM NaCl, and 18-28% w/v PEG 3350, pyruvate complexes of the wild-type and K165-gamma-thialysine mutant enzymes crystals are soaked in the mother liquor containing 100 mM sodium pyruvate and 15% v/v PEG 400 for 1 min before being sequentially transferred to mother liquor with 5% increments in PEG 400 concentration. The final soak contains the mother liquor containing 100 mM sodium pyruvate and 25% v/v PEG 400, 18°C, X-ray diffraction structure determination and analysis at about 2.0 A resolution, molecular replacement
Staphylococcus aureus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
C118A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C118S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C238A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C238S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C270A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C270S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C82A
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
C82S
site-directed mutagenesis, the mutant shows kinetic properties identical to the wild-type enzyme
Staphylococcus aureus
K165C
site-directed mutagenesis to introduce a cysteine in place of Lys165 in the enzyme active site and complete conversion of the cysteine into gamma-thialysine through dehydroalanine as by chemical mutagenesis, ESI-mass spectrometry and kinetic characterisation, the K165C variant is severely impaired in catalysis, kcat/Km is reduced 720fold compared with wild-type
Staphylococcus aureus
K165Dha
site-directed mutagenesis to introduce a cysteine in place of Lys165 in the enzyme active site and complete conversion of the cysteine into gamma-thialysine, Dha, through dehydroalanine as by chemical mutagenesis, ESI-mass spectrometry and kinetic characterisation, the enzyme containing gamma-thialysine regains 17-30% of the wild-type activity
Staphylococcus aureus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.013
-
N-acetylneuraminate
purified recombinant mutant K165C, pH 7.4, 30°C
Staphylococcus aureus
0.015
-
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 6.8, 30°C
Staphylococcus aureus
0.023
-
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 7.4, 30°C
Staphylococcus aureus
0.036
-
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 7.4, 30°C
Staphylococcus aureus
0.04
-
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 6.8, 30°C
Staphylococcus aureus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33992
-
x * 33992, recombinant His6-tagged wild-type enzyme, mass spectrometry
Staphylococcus aureus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
N-acetylneuraminate
Staphylococcus aureus
-
N-acetyl-D-mannosamine + pyruvate
-
-
r
N-acetylneuraminate
Staphylococcus aureus NCTC 8325
-
N-acetyl-D-mannosamine + pyruvate
-
-
r
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Staphylococcus aureus
Renatured (Commentary) (protein specific)
Commentary
Organism
recombinant wild-type enzyme with various concentrations of urea in Tris·HCl buffer, 50 mM, pH 7.4, the refolded enzyme shows higher activity than the native wild-type enzyme
Staphylococcus aureus
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.33
-
purified recombinant wild-type enzyme, pH 7.4, 30°C
Staphylococcus aureus
6
-
purified recombinant refolded wild-type enzyme, pH 7.4, 30°C
Staphylococcus aureus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
N-acetylneuraminate
-
727317
Staphylococcus aureus
N-acetyl-D-mannosamine + pyruvate
-
-
-
r
N-acetylneuraminate
-
727317
Staphylococcus aureus NCTC 8325
N-acetyl-D-mannosamine + pyruvate
-
-
-
r
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 33992, recombinant His6-tagged wild-type enzyme, mass spectrometry
Staphylococcus aureus
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Staphylococcus aureus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.013
-
N-acetylneuraminate
purified recombinant mutant K165C, pH 7.4, 30°C
Staphylococcus aureus
0.015
-
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 6.8, 30°C
Staphylococcus aureus
0.023
-
N-acetylneuraminate
purified recombinant mutant K165-gamma-thialysine, pH 7.4, 30°C
Staphylococcus aureus
0.036
-
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 7.4, 30°C
Staphylococcus aureus
0.04
-
N-acetylneuraminate
purified recombinant wild-type enzyme, pH 6.8, 30°C
Staphylococcus aureus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6.8
-
mutant K165-gamma-thialysine
Staphylococcus aureus
7.4
-
wild-type enzyme
Staphylococcus aureus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
5
10
pH-activity profiles of the wild-type enzyme, overview
Staphylococcus aureus
6
9
pH-activity profiles of the K165-gamma-thialysine mutant enzyme, overview
Staphylococcus aureus
Other publictions for EC 4.1.3.3
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
748534
Wang
Molecular characterization of ...
Mycoplasma sp.
Mar. Drugs
16
E80
2018
2
1
1
-
3
1
4
3
-
4
-
1
-
2
-
-
-
-
-
-
-
-
2
1
2
-
1
-
2
-
1
-
-
-
-
2
1
1
-
-
3
1
-
4
-
3
-
4
-
1
-
-
-
-
-
-
-
-
2
1
2
-
1
-
2
-
1
-
-
-
-
-
3
3
748013
Wang
In vivo multienzyme complex c ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
J. Agric. Food Chem.
65
7467-7475
2017
-
-
1
-
-
-
-
-
-
-
-
2
-
28
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
747776
North
Structure and inhibition of N ...
Staphylococcus aureus, Staphylococcus aureus NCTC 8325
FEBS Lett.
590
4414-4428
2016
-
-
-
1
-
-
1
1
-
-
1
2
-
5
-
-
-
-
-
-
-
-
2
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
1
1
1
-
-
1
2
-
-
-
-
-
-
-
-
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
749312
Ji
Characterization of a novel N ...
Corynebacterium glutamicum, Corynebacterium glutamicum ATCC 13032
Sci. Rep.
5
9341
2015
2
-
1
-
-
-
3
6
-
5
-
2
-
3
-
-
1
-
-
-
-
-
4
1
3
-
1
6
2
-
-
-
-
-
-
2
-
1
-
-
-
-
-
3
-
6
-
5
-
2
-
-
-
1
-
-
-
-
4
1
3
-
1
6
2
-
-
-
-
-
-
-
6
6
726551
Daniels
Reaction mechanism of N-acetyl ...
Haemophilus influenzae
ACS Chem. Biol.
9
1025-1032
2014
-
-
-
1
13
-
-
2
-
-
-
1
-
3
-
-
-
1
-
-
-
-
2
-
1
-
-
2
1
-
-
-
-
-
-
-
-
-
-
1
13
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
2
1
-
-
-
-
2
2
-
2
2
749150
Garcia-Garcia
First functional and mutation ...
Lactobacillus antri, Lactobacillus antri DSMZ 16041, Lactobacillus sakei 23K, Lactobacillus sakei
PLoS ONE
9
e96976
2014
-
-
2
-
3
-
-
13
-
-
2
4
-
5
-
-
2
-
-
-
-
-
22
2
3
-
2
13
2
-
-
-
-
-
-
-
-
2
-
-
3
-
-
-
-
13
-
-
2
4
-
-
-
2
-
-
-
-
22
2
3
-
2
13
2
-
-
-
-
-
-
-
13
13
726631
North
Cloning, expression, purificat ...
Staphylococcus aureus, Staphylococcus aureus MRSA252
Acta Crystallogr. Sect. F
69
306-312
2013
-
-
1
1
-
-
-
-
-
-
-
2
-
5
-
-
1
-
-
-
1
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
1
-
-
1
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
727035
Huynh
Structural basis for substrate ...
Pasteurella multocida
Biochemistry
52
8570-8579
2013
-
-
1
1
1
-
-
-
-
-
1
-
-
3
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
1
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
727186
Sun
Construction and expression of ...
Escherichia coli
Biores. Technol.
130
23-29
2013
-
-
1
-
1
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
727317
Timms
Structural insights into the r ...
Staphylococcus aureus, Staphylococcus aureus NCTC 8325
ChemBioChem
14
474-481
2013
-
-
1
1
10
-
-
5
-
-
1
2
-
4
-
-
1
-
1
-
2
-
2
1
1
-
-
5
2
2
-
-
-
-
-
-
-
1
-
1
10
-
-
-
-
5
-
-
1
2
-
-
-
1
1
-
2
-
2
1
1
-
-
5
2
2
-
-
-
-
-
-
-
-
727332
Zhou
Molecular cloning and characte ...
Staphylococcus hominis
Chin. J. Biotechnol.
29
480-489
2013
-
-
1
-
-
-
-
3
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
1
-
2
-
2
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
2
-
2
-
1
-
-
-
-
-
3
3
728608
Xiao
Progesterone receptor-mediated ...
Mus musculus, Mus musculus B6/129S5-NplGt(IRESBetageo)332Lex/Mmucd
PLoS ONE
8
e65607
2013
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
3
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
2
1
1
2
-
-
727656
Garcia Garcia
Characterization of a novel N- ...
Staphylococcus carnosus, Staphylococcus carnosus TM300
J. Agric. Food Chem.
60
7450-7456
2012
-
1
1
-
-
-
-
3
-
-
-
4
-
5
-
-
1
-
-
-
1
-
4
-
2
1
4
3
1
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
3
-
-
-
4
-
-
-
1
-
-
1
-
4
-
2
1
4
3
1
-
-
-
-
-
-
-
3
3
713843
Sanchez-Carron
Molecular characterization of ...
Lactobacillus plantarum
Appl. Environ. Microbiol.
77
2471-2478
2011
-
-
1
-
-
1
-
3
-
-
2
-
-
3
-
-
1
-
-
-
1
-
1
1
2
-
2
-
1
1
1
-
-
-
-
-
-
1
-
-
-
1
-
-
-
3
-
-
2
-
-
-
-
1
-
-
1
-
1
1
2
-
2
-
1
1
1
-
-
-
-
-
3
3
713852
Gao
Chemoenzymatic synthesis of N- ...
Escherichia coli
Appl. Environ. Microbiol.
77
7080-7083
2011
-
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
-
-
714508
Garcia-Garcia
New stabilized FastPrep-CLEAs ...
Lactobacillus plantarum, Lactobacillus plantarum WFCS1
Biores. Technol.
102
6186-6191
2011
-
1
1
-
-
-
-
4
-
-
-
-
-
3
-
-
1
-
-
-
-
-
2
-
-
-
1
-
2
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
4
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
1
-
2
-
-
-
-
-
-
-
4
4
701855
Hu
Coupled bioconversion for prep ...
Escherichia coli, Escherichia coli TG1, Sus scrofa
Appl. Microbiol. Biotechnol.
85
1383-1391
2010
-
1
2
-
-
1
-
-
-
-
-
1
-
7
-
-
2
-
-
1
5
-
3
-
1
-
-
-
-
-
-
-
-
-
-
-
1
2
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
2
-
1
5
-
3
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
701881
Zhang
An efficient method for N-acet ...
Escherichia coli
Appl. Microbiol. Biotechnol.
86
481-489
2010
-
1
1
-
-
-
-
-
-
-
1
1
-
4
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
715921
Campeotto
Structural insights into subst ...
Escherichia coli
J. Mol. Biol.
404
56-69
2010
-
-
1
1
19
-
1
17
-
-
-
-
-
2
-
-
1
-
-
-
-
-
3
-
-
-
-
18
-
-
-
-
1
-
-
-
-
1
-
1
19
-
-
1
1
17
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
18
-
-
-
-
-
-
-
-
19
19
693709
Chu
Homology modeling and molecula ...
Homo sapiens
J. Mol. Model.
15
323-328
2009
-
-
-
-
-
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
701496
Campeotto
Structure of an Escherichia co ...
Escherichia coli
Acta Crystallogr. Sect. F
65
1088-1090
2009
-
-
-
1
1
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
702067
Devenish
The quaternary structure of Es ...
Escherichia coli, Escherichia coli W3110 / ATCC 27325
Biochem. Biophys. Res. Commun.
388
107-111
2009
-
-
1
-
18
-
-
11
-
-
1
-
-
3
-
-
1
-
-
-
-
-
2
1
-
-
1
11
-
-
-
-
-
-
-
-
-
1
-
-
18
-
-
-
-
11
-
-
1
-
-
-
-
1
-
-
-
-
2
1
-
-
1
11
-
-
-
-
-
1
1
-
-
-
690576
Li
Pasteurella multocida sialic a ...
Escherichia coli K-12, Pasteurella multocida
Appl. Microbiol. Biotechnol.
79
963-970
2008
-
-
2
-
-
-
-
6
-
-
4
2
-
4
-
-
2
-
-
-
-
-
3
-
2
-
-
6
2
2
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
6
-
-
4
2
-
-
-
2
-
-
-
-
3
-
2
-
-
6
2
2
-
-
-
-
-
-
-
-
674987
Lee
Production of N-acetyl-D-neura ...
Escherichia coli
J. Biotechnol.
129
453-460
2007
-
-
1
-
-
-
-
-
-
-
1
-
-
6
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
677556
Huang
Disaccharides as sialic acid a ...
Escherichia coli
Angew. Chem. Int. Ed. Engl.
46
2249-2253
2007
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
682313
Paccalet
Engineering of a sialic acid s ...
Escherichia coli, Escherichia coli K1
Plant Biotechnol. J.
5
16-25
2007
-
-
1
-
-
-
-
-
-
-
1
-
-
14
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
678004
Wang
-
Production of 2-keto-3-deoxy-D ...
Escherichia coli
Biochem. Eng. J.
29
75-80
2006
-
-
1
-
-
-
-
1
-
-
2
-
-
1
-
-
1
-
-
-
2
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
1
-
-
2
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
682230
Yu
Aldolase-catalyzed synthesis o ...
Escherichia coli
Org. Lett.
8
2393-2396
2006
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
663630
Woodhall
Creation of a tailored aldolas ...
Haemophilus influenzae
Angew. Chem.
44
2109-2112
2005
-
-
-
-
1
-
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
664734
Wu
A novel splice variant of huma ...
Homo sapiens
DNA Seq.
16
137-142
2005
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
666750
Hsu
Directed evolution of D-sialic ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
102
9122-9126
2005
-
-
-
-
6
-
-
23
-
-
-
-
-
1
-
-
-
-
-
-
-
-
17
-
-
-
-
21
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
23
-
-
-
-
-
-
-
-
-
-
-
-
17
-
-
-
-
21
-
-
-
-
-
-
-
-
-
-
666805
Williams
Structure-guided saturation mu ...
Escherichia coli
Protein Eng. Des. Sel.
18
239-246
2005
-
-
-
-
5
-
-
11
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
11
-
-
-
-
-
-
-
-
-
-
-
-
5
-
-
-
-
11
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
11
-
-
-
-
-
-
-
-
-
-
661608
Lee
-
Production of N-acetylneuramin ...
Escherichia coli
Enzyme Microb. Technol.
35
121-125
2004
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
666956
Lins
-
Generation of a dynamic combin ...
Clostridium perfringens
Tetrahedron
60
771-780
2004
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
650525
Wada
Directed evolution of N-acetyl ...
Escherichia coli
Bioorg. Med. Chem.
11
2091-2098
2003
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
653594
Joerger
Mimicking natural evolution in ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
100
5694-5699
2003
-
-
-
1
2
-
1
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
1
2
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
650772
Kok
Synthesis of C-3 nitrogen-cont ...
Escherichia coli
Carbohydr. Res.
332
133-139
2001
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
651103
Kruger
Characterization and mutagenes ...
Clostridium perfringens
Eur. J. Biochem.
268
3831-3839
2001
-
-
1
-
9
-
-
11
-
-
1
-
-
3
-
-
1
1
-
-
1
-
2
-
1
-
2
-
1
-
-
-
-
-
-
-
-
1
-
-
9
-
-
-
-
11
-
-
1
-
-
-
-
1
-
-
1
-
2
-
1
-
2
-
1
-
-
-
-
-
-
-
-
-
652833
Barbosa
Active Site Modulation in the ...
Haemophilus influenzae, Homo sapiens
J. Mol. Biol.
303
405-421
2000
-
-
-
1
-
-
3
1
1
-
-
1
-
3
-
-
-
1
-
-
-
-
4
-
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
1
-
-
-
3
1
1
1
-
-
1
-
-
-
-
-
-
-
-
4
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
650651
Schauer
The terminal enzymes of sialic ...
Clostridium perfringens, Sus scrofa
Biosci. Rep.
19
373-383
1999
-
-
-
-
-
-
19
2
-
-
1
-
-
2
-
-
-
2
-
-
2
-
8
2
2
-
-
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
-
19
-
2
-
-
1
-
-
-
-
-
-
-
2
-
8
2
2
-
-
-
2
-
-
2
-
-
-
-
-
-
651432
Sommer
The sialate pyruvate-lyase fro ...
Sus scrofa
Glycoconj. J.
16
425-435
1999
-
-
-
-
-
-
4
2
-
1
1
-
-
1
-
-
1
-
-
-
1
-
3
2
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
4
-
2
-
1
1
-
-
-
-
1
-
-
1
-
3
2
1
-
-
-
1
-
-
1
-
-
-
-
-
-
652991
Smith
Substrate-assisted catalysis i ...
Haemophilus influenzae
J. Org. Chem.
64
945-949
1999
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
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-
-
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-
33325
Lilley
Expression in Escherichia coli ...
Clostridium perfringens, Haemophilus influenzae
Protein Expr. Purif.
12
295-304
1998
-
-
1
1
-
-
-
-
-
-
-
-
-
4
-
-
1
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2
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-
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-
-
-
-
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-
-
-
-
33334
Maru
Simple and large-scale product ...
Escherichia coli
Carbohydr. Res.
306
575-578
1998
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
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-
-
-
-
-
-
-
-
-
-
33331
Yamamoto
Serratia liquefaciens as a new ...
Escherichia coli
Anal. Biochem.
246
171-175
1997
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
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-
33335
Mahmoudian
An efficient process for produ ...
Escherichia coli
Enzyme Microb. Technol.
20
393-400
1997
-
1
-
-
-
-
-
-
-
-
-
-
-
3
-
-
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-
-
-
-
-
-
-
-
-
-
658576
Mahmoudian
-
An efficient process for produ ...
Escherichia coli
Enzyme Microb. Technol.
45
393-400
1997
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
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1
-
1
-
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-
1
-
-
-
-
-
-
-
-
-
33321
Schauer
Isolation and characterization ...
Sus scrofa
Biol. Chem. Hoppe-Seyler
377
293-299
1996
-
-
-
-
-
-
7
1
-
-
2
-
-
3
1
-
-
-
-
2
1
-
4
-
-
-
-
-
1
-
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-
-
-
-
-
-
-
-
-
-
-
7
-
1
-
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2
-
-
1
-
-
-
2
1
-
4
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
33337
Ferrero
N-acetyl-D-neuraminic acid lya ...
Escherichia coli
Biochem. J.
317
157-165
1996
-
-
-
-
-
-
6
4
-
-
1
1
-
4
-
-
1
-
-
-
1
1
4
1
1
-
3
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
4
-
-
1
1
-
-
-
1
-
-
1
1
4
1
1
-
3
-
1
-
-
-
-
-
-
-
-
-
33318
Mueller
Occurence of sialidase and N-a ...
Pasteurella sp.
Zentralbl. Bakteriol.
283
105-114
1995
-
-
-
-
-
-
-
-
-
-
-
1
-
5
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
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-
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-
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-
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-
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-
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-
1
-
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33333
Izard
The three-dimensional structur ...
Escherichia coli
Structure
2
361-369
1994
-
-
-
1
-
-
-
-
-
-
-
1
-
3
-
-
-
-
-
-
-
-
3
1
-
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-
-
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1
-
-
-
-
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-
-
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-
1
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-
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-
-
-
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33336
Lilley
High-level production and puri ...
Escherichia coli
Protein Expr. Purif.
3
434-440
1992
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33332
Aisaka
Purification, crystallization ...
Escherichia coli
Biochem. J.
276
541-546
1991
-
-
-
1
-
-
9
2
-
-
2
-
-
2
1
-
1
-
-
-
1
-
1
1
1
-
1
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
9
-
2
-
-
2
-
-
1
-
1
-
-
1
-
1
1
1
-
1
-
1
-
1
-
-
-
-
-
-
-
33322
Gross
Inhibition of N-acetylneuramin ...
Clostridium perfringens, Escherichia coli
FEBS Lett.
232
145-147
1988
-
-
-
-
-
-
2
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33323
Aisaka
-
Hyperproduction of N-acetylneu ...
Escherichia coli
Biotechnol. Lett.
9
633-637
1987
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
33324
Ohta
-
Molecular cloning of the N-ace ...
Escherichia coli
Appl. Microbiol. Biotechnol.
24
386-391
1986
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33314
Uchida
Purification and properties of ...
Escherichia coli
J. Biochem.
96
507-522
1984
-
1
-
-
-
-
8
2
-
1
2
-
-
3
1
-
1
-
-
1
2
-
4
1
1
1
3
-
1
1
1
-
-
-
-
-
1
-
-
-
-
-
-
8
-
2
-
1
2
-
-
1
-
1
-
1
2
-
4
1
1
1
3
-
1
1
1
-
-
-
-
-
-
-
33327
Deijl
Configuration of substrate and ...
Clostridium perfringens
Biochem. Biophys. Res. Commun.
111
668-674
1983
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
33329
Kolisis
The protection role of pyruvat ...
Clostridium perfringens
FEBS Lett.
121
280-282
1980
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
33315
Nees
Purification and characterizat ...
Clostridium perfringens
Hoppe-Seyler's Z. Physiol. Chem.
357
839-853
1976
-
-
-
-
-
-
5
2
1
1
3
-
-
4
-
-
1
1
-
-
-
-
2
1
1
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
5
-
2
1
1
3
-
-
-
-
1
-
-
-
-
2
1
1
-
-
1
1
-
-
-
-
-
-
-
-
-
33320
Barnett
The reaction of N-acetylneuram ...
Clostridium perfringens
Biochem. J.
143
487-490
1974
-
-
-
-
-
-
1
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33316
DeVries
N-acetylneuraminic acid aldola ...
Clostridium perfringens
Arch. Biochem. Biophys.
151
234-242
1972
-
-
-
-
-
-
9
1
-
1
1
-
-
2
-
-
1
-
-
-
1
-
2
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
9
-
1
-
1
1
-
-
-
-
1
-
-
1
-
2
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
33326
Arden
Distribution of neuraminidase ...
Corynebacterium belfanti, Corynebacterium diphtheriae, Corynebacterium pseudotuberculosis, Corynebacterium ulcerans
J. Bacteriol.
112
1206-1212
1972
-
-
-
-
-
-
-
-
1
-
-
4
-
5
-
-
-
-
-
-
-
-
8
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
8
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
33317
Barnett
Studies on N-acetylneuraminic ...
Clostridium perfringens
Biochem. J.
125
275-285
1971
-
-
-
-
-
-
3
1
-
1
1
-
-
1
-
-
1
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
1
-
1
1
-
-
-
-
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
33328
Schauer
Studies on the substrate speci ...
Clostridium perfringens
Hoppe-Seyler's Z. Physiol. Chem.
352
1073-1080
1971
-
-
-
-
-
-
2
10
-
-
-
-
-
1
-
-
-
-
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
10
-
-
-
-
-
-
-
-
-
-
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
33319
Sirbasku
Purification and properties of ...
Bos taurus
Biochim. Biophys. Acta
198
479-482
1970
-
-
-
-
-
-
4
1
-
-
1
-
-
2
-
-
1
-
-
2
1
-
2
-
-
-
1
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
4
2
1
-
-
1
-
-
-
-
1
-
2
1
-
2
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
33330
Comb
The sialic acids. I. Structure ...
Escherichia coli, Rattus norvegicus
J. Biol. Chem.
235
2529-2537
1960
-
-
-
-
-
-
-
1
-
-
-
1
-
2
-
-
1
-
-
2
1
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
1
-
2
1
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-